ACON2_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ACON2_YEAST
• UniProt AC: P39533
• Protein Name: Homocitrate dehydratase, mitochondrial
• Gene Name: ACO2
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 789
• Subcellular Localization: Mitochondrion .
• Protein Description: Catalyzes the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis..
• Protein Sequence: MLSSANRFYIKRHLATHANMFPSVSKNFQTKVPPYAKLLTNLDKIKQITNNAPLTLAEKILYSHLCDPEESITSSDLSTIRGNKYLKLNPDRVAMQDASAQMALLQFMTTGLNQTSVPASIHCDHLIVGKDGETKDLPSSIATNQEVFDFLESCAKRYGIQFWGPGSGIIHQIVLENFSAPGLMMLGTDSHTPNAGGLGAIAIGVGGADAVDALTGTPWELKAPKILGVKLTGKLNGWSTPKDVITKLAGLLTVRGGTGYIVEYFGEGVSTLSCTGMATICNMGAEIGATTSTFPYQEAHKRYLQATNRAEVAEAADVALNKFNFLRADKDAQYDKVIEIDLSAIEPHVNGPFTPDLSTPISQYAEKSLKENWPQKVSAGLIGSCTNSSYQDMSRVVDLVKQASKAGLKPRIPFFVTPGSEQIRATLERDGIIDIFQENGAKVLANACGPCIGQWNREDVSKTSKETNTIFTSFNRNFRARNDGNRNTMNFLTSPEIVTAMSYSGDAQFNPLTDSIKLPNGKDFKFQPPKGDELPKRGFEHGRDKFYPEMDPKPDSNVEIKVDPNSDRLQLLEPFKPWNGKELKTNVLLKVEGKCTTDHISAAGVWLKYKGHLENISYNTLIGAQNKETGEVNKAYDLDGTEYDIPGLMMKWKSDGRPWTVIAEHNYGEGSAREHAALSPRFLGGEILLVKSFARIHETNLKKQGVLPLTFANESDYDKISSGDVLETLNLVDMIAKDGNNGGEIDVKITKPNGESFTIKAKHTMSKDQIDFFKAGSAINYIGNIRRNE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
44	Acetylation	KLLTNLDKIKQITNN HHHHCHHHHHHHHCC	55.77	24489116
66	Glutathionylation	KILYSHLCDPEESIT HHHHHHHCCHHHHCC	7.40	22833525
154	Glutathionylation	VFDFLESCAKRYGIQ HHHHHHHHHHHHCCC	3.65	22833525
234	Acetylation	LGVKLTGKLNGWSTP ECEECEEECCCCCCC	33.28	24489116
247	Acetylation	TPKDVITKLAGLLTV CCHHHHHHHHCCEEE	25.80	24489116
322	Acetylation	AADVALNKFNFLRAD HHHHHHHHCCCCCCC	42.40	25381059
370	Acetylation	QYAEKSLKENWPQKV HHHHHHHHHHCCCCC	56.97	25381059
388	Phosphorylation	LIGSCTNSSYQDMSR HHHHHCCCCHHHHHH	16.57	28889911
401	Acetylation	SRVVDLVKQASKAGL HHHHHHHHHHHHCCC	47.66	25381059
448	Glutathionylation	AKVLANACGPCIGQW CHHHHHHHHCCCCCC	6.66	22833525
451	Glutathionylation	LANACGPCIGQWNRE HHHHHHCCCCCCCHH	3.11	22833525
462	Acetylation	WNREDVSKTSKETNT CCHHHHHHHCCHHCC	57.58	25381059
522	Acetylation	SIKLPNGKDFKFQPP CEECCCCCCCCCCCC	67.63	25381059
545	Acetylation	GFEHGRDKFYPEMDP CCCCCCCCCCCCCCC	45.49	24489116
581	Acetylation	PFKPWNGKELKTNVL CCCCCCCCCCCCCEE	57.57	24489116
584	Acetylation	PWNGKELKTNVLLKV CCCCCCCCCCEEEEE	38.86	25381059
590	Acetylation	LKTNVLLKVEGKCTT CCCCEEEEEECEECC	33.79	24489116
608	Acetylation	SAAGVWLKYKGHLEN EECCEEEEECCCCEE	29.24	25381059
610	Acetylation	AGVWLKYKGHLENIS CCEEEEECCCCEEEE	37.96	25381059
710	Phosphorylation	KQGVLPLTFANESDY HCCCEEEEECCHHHC	20.82	21126336
715	Phosphorylation	PLTFANESDYDKISS EEEECCHHHCCCCCC	41.08	21126336
767	Acetylation	KAKHTMSKDQIDFFK EEEECCCHHHHCEEH	42.71	24489116

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ACON2_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ACON2_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ACON2_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACON2_YEAST	ACO2	physical	22940862

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.